MUHAMMAD IZZUL BIN ZAINOL ALAM (A153832)

Compounds found in biological systems which are d block elements.

The first element is Iron (Fe). This element easily find in a compound
in our bodies. For example is ferritin. Ferritin is water-soluble
metalloprotein in which the Fe is stored in the liver, bone marrow and
spleen. It functions as a buffer against Fe deficiency and avoid iron
overload by control Fe in our body.

Image 1.1) Chemical Structure of Ferritin

Next, the most common compound in the body which involved Fe is
heme group. This important both for haemoglobin and myoglobin because
each heme consists one iron element that side of attach for oxygen. So for
haemoglobin have 4 heme and hold 4 oxygen at once time. Fe also affect
by adjust the conformational of haemoglobin if oxygen absent and
present.

Image 1.2) Chemical structure of Heme group

Iron (Fe) also important in cytochrome, which interconvert between
Fe and Fe3+ states for either electron-transfer processes or oxidative
processes. This makes cytochrome capable of performing oxidation and
reduction. This efficiency really helps in the oxidative phosphorylation
process which involve electron transfer and as result ATP production is
flow nicer
2+

Besides that, an element like cobalt also has a compound that related
to biological systems. Cobalt is one of element that made up Vitamin B12. This is
important vitamin in maintain metabolism of organisms. It help in anaemia,
vitamin B12 deficiency and also cyanide poisoning. Cobalt is refer as central
metal ion in Vitamin B12. Cobalt help in catalytic activity and make cobalt cycles
between Co,Co and Co.

Image 1.3 ) Chemical structure of Vitamin B12.

Next compound which have d-block element is haemocyanin which
contain copper. Unlike homosapien, Mollusca and Anthtopoda use hemocyanins
that have two copper in centre and can bind to single oxygen(O). This use by
few insect to direct transfer oxygen to tissue.

Lastly, element like Zinc (Zn) also attach toward some compound which
involve in biological system. Zinc in proteins can either participate directly in

chemical catalysis or be important for maintaining protein structure and

stability. In all catalytic sites, the zinc ion functions as a Lewis acid.
Researchers in our laboratory are dissecting the determinants of
molecular recognition and catalysis in the zinc-binding site of carbonic

anhydrase. These studies demonstrate that the chemical nature of the

direct ligands and the structure of the surrounding hydrogen bond
network are crucial for both the activity of carbonic anhydrase and the
metal ion affinity of the zinc-binding site. An understanding of naturally
occurring zinc-binding sites will aid in creating de novo zinc-binding
proteins and in designing new metal sites in existing proteins for novel
purposes such as to serve as metal ion biosensors.